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Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement
Transient structures in unfolded proteins are important in elucidating the molecular details of initiation of protein folding. Recently, native and non-native secondary structure have been discovered in unfolded A. vinelandii flavodoxin. These structured elements transiently interact and subsequentl...
| Autores principales: | , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Springer-Verlag
2009
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2841281/ https://www.ncbi.nlm.nih.gov/pubmed/19894043 http://dx.doi.org/10.1007/s00249-009-0556-4 |